Daoxiang Chen, Hui Liu, Xinhua Liu, Haixin Jing, Xijun Lian
{"title":"小麦直链淀粉对尿素溶性谷蛋白中二硫键形成的影响","authors":"Daoxiang Chen, Hui Liu, Xinhua Liu, Haixin Jing, Xijun Lian","doi":"10.1007/s11947-024-03580-0","DOIUrl":null,"url":null,"abstract":"<p>The addition of excessive amylose to the dough leads to a deterioration in the quality of the gluten network. Disulfide bond is the main factor influencing the quality of gluten network structure. In this paper, wheat amylose was mixed with urea-soluble glutenin (USG) under different conditions to investigate its effects on the disulfide bond formation of USG. The results showed that the addition of 5% wheat amylose stirred at 45 ℃ for 1 h could sharply increase the disulfide bond contents of USG from 0.85 to 4.35%. The results of microscopy showed that the formation of wheat amylose/USG gel was unfavorable/favorable to the formation of the disulfide bond in complex. FTIR and <sup>13</sup>C solid-state NMR results showed that the α-helix secondary structure of USG was transformed into intermolecular β-sheet and β-turn after mixing with wheat amylose. Ser of USG interacted with wheat amylose through dehydration condensation and hydrogen bonds formed between Pro of USG and C2, 3, 5, 6 of wheat amylose during the interaction of both. The X-ray diffraction pattern of USG was 2<i>θ 22.06°</i>, <i>23.56°</i>, <i>29.10°</i>, and <i>35.30°</i>, and they all disappeared after mixing with wheat amylose. USG with the highest disulfide bond contents in complex showed lower peak denaturation temperature and melting enthalpy. A possible interaction way of wheat amylose and USG was deduced. Wheat amylose could regulate the disulfide bond formation of USG under appropriate conditions.</p>","PeriodicalId":562,"journal":{"name":"Food and Bioprocess Technology","volume":"12 1","pages":""},"PeriodicalIF":5.3000,"publicationDate":"2024-09-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Effects of Wheat Amylose on the Formation of Disulfide Bonds in Urea-Soluble Glutenin\",\"authors\":\"Daoxiang Chen, Hui Liu, Xinhua Liu, Haixin Jing, Xijun Lian\",\"doi\":\"10.1007/s11947-024-03580-0\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p>The addition of excessive amylose to the dough leads to a deterioration in the quality of the gluten network. Disulfide bond is the main factor influencing the quality of gluten network structure. In this paper, wheat amylose was mixed with urea-soluble glutenin (USG) under different conditions to investigate its effects on the disulfide bond formation of USG. The results showed that the addition of 5% wheat amylose stirred at 45 ℃ for 1 h could sharply increase the disulfide bond contents of USG from 0.85 to 4.35%. The results of microscopy showed that the formation of wheat amylose/USG gel was unfavorable/favorable to the formation of the disulfide bond in complex. FTIR and <sup>13</sup>C solid-state NMR results showed that the α-helix secondary structure of USG was transformed into intermolecular β-sheet and β-turn after mixing with wheat amylose. Ser of USG interacted with wheat amylose through dehydration condensation and hydrogen bonds formed between Pro of USG and C2, 3, 5, 6 of wheat amylose during the interaction of both. The X-ray diffraction pattern of USG was 2<i>θ 22.06°</i>, <i>23.56°</i>, <i>29.10°</i>, and <i>35.30°</i>, and they all disappeared after mixing with wheat amylose. USG with the highest disulfide bond contents in complex showed lower peak denaturation temperature and melting enthalpy. A possible interaction way of wheat amylose and USG was deduced. Wheat amylose could regulate the disulfide bond formation of USG under appropriate conditions.</p>\",\"PeriodicalId\":562,\"journal\":{\"name\":\"Food and Bioprocess Technology\",\"volume\":\"12 1\",\"pages\":\"\"},\"PeriodicalIF\":5.3000,\"publicationDate\":\"2024-09-03\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Food and Bioprocess Technology\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://doi.org/10.1007/s11947-024-03580-0\",\"RegionNum\":2,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"FOOD SCIENCE & TECHNOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food and Bioprocess Technology","FirstCategoryId":"97","ListUrlMain":"https://doi.org/10.1007/s11947-024-03580-0","RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"FOOD SCIENCE & TECHNOLOGY","Score":null,"Total":0}
Effects of Wheat Amylose on the Formation of Disulfide Bonds in Urea-Soluble Glutenin
The addition of excessive amylose to the dough leads to a deterioration in the quality of the gluten network. Disulfide bond is the main factor influencing the quality of gluten network structure. In this paper, wheat amylose was mixed with urea-soluble glutenin (USG) under different conditions to investigate its effects on the disulfide bond formation of USG. The results showed that the addition of 5% wheat amylose stirred at 45 ℃ for 1 h could sharply increase the disulfide bond contents of USG from 0.85 to 4.35%. The results of microscopy showed that the formation of wheat amylose/USG gel was unfavorable/favorable to the formation of the disulfide bond in complex. FTIR and 13C solid-state NMR results showed that the α-helix secondary structure of USG was transformed into intermolecular β-sheet and β-turn after mixing with wheat amylose. Ser of USG interacted with wheat amylose through dehydration condensation and hydrogen bonds formed between Pro of USG and C2, 3, 5, 6 of wheat amylose during the interaction of both. The X-ray diffraction pattern of USG was 2θ 22.06°, 23.56°, 29.10°, and 35.30°, and they all disappeared after mixing with wheat amylose. USG with the highest disulfide bond contents in complex showed lower peak denaturation temperature and melting enthalpy. A possible interaction way of wheat amylose and USG was deduced. Wheat amylose could regulate the disulfide bond formation of USG under appropriate conditions.
期刊介绍:
Food and Bioprocess Technology provides an effective and timely platform for cutting-edge high quality original papers in the engineering and science of all types of food processing technologies, from the original food supply source to the consumer’s dinner table. It aims to be a leading international journal for the multidisciplinary agri-food research community.
The journal focuses especially on experimental or theoretical research findings that have the potential for helping the agri-food industry to improve process efficiency, enhance product quality and, extend shelf-life of fresh and processed agri-food products. The editors present critical reviews on new perspectives to established processes, innovative and emerging technologies, and trends and future research in food and bioproducts processing. The journal also publishes short communications for rapidly disseminating preliminary results, letters to the Editor on recent developments and controversy, and book reviews.